Research workbench
AlphaFold monomer V2.0 prediction for glutamine--tRNA ligase (A5F2T1)
Analyse AlphaFold monomer V2.0 prediction for glutamine--tRNA ligase (A5F2T1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5F2T1
- Type
- protein
- Length
- 556 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- Molecule
- Glutamine--tRNA ligase
- UniProt
- A5F2T1
- Pockets
- 5 · best druggability 0.67
Structure
1 distinct chain · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine--tRNA ligase | protein | 556 | 32% helix, 25% strand | A5F2T1 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 359 | 0.67 | 0.81 | 32 | empty |
| 2 | 130 | 0.49 | 0.79 | 17 | empty |
| 3 | 180 | 0.42 | 0.73 | 20 | empty |
| 4 | 73 | 0.36 | 0.77 | 15 | empty |
| 5 | 98 | 0.36 | 0.75 | 21 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A5F2T1
- Elsewhere: UniProt A5F2T1 · AlphaFold DB A5F2T1
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